Related Experiment Video
Updated: Aug 19, 2026

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
Published on: May 9, 2016
[Study of the nucleation sites in collagen mineralization]
Zhao-long Huang1, Wei Zhang, Fu-zhai Cui
1Department of Materials Science and Engineering, Tsinghua University, Beijing 100084, China.
Abstract:
By comparing IR spectra of collagen, collagen/CaCl2 and collagen/calcium phosphate, it was found that intensities of amide I, II and III bands were significantly decreased after mineralization. Band amide I shifted to wards lower wave number. This shift indicated chemical interaction between carboxyl groups and Ca ions formed in the mineralization. The result indicated that there was another nucleation site, i.e. carbonyl [structure: see text] on collagen, besides the previous reported nucleation site of carboxyl (-COOH) on collagen. The decrease of amide I peak intensity was mainly due to blockage of C=O stretch. Comparing the IR spectra of demineralized collagen and pure collagen, amide I, II and III peaks intensity and position were almost the same. When the mineral dissolved, amide peaks rebounded, which indicated that the crystals nucleated on these sites enwrapped the groups and blocked the groups vibration. The decreases of peak intensity of amide I, II and III were different due to their different vibration modes. The result confirmed that the carbonyl group was one kind of the nucleation site during collagen mineralization. The relationship between the process of collagen mineralization and variety of amide bonds was also studied.
Related Concept Videos
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Type IV Collagen of Basal Lamina
A type IV collagen molecule has six alpha chains which can exist in...
Fibril-associated Collagen
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
